In normal dogs and in dogs treated with 20 or 30 U.S.P. parathyroid extract for 5 and 34 days, respectively, the glycosaminoglyeans of compact bone tissue were identified using the cetylpyridinium chloride precipitation method, and the concentrations of total hexosamines and the hexosamines corresponding to cetylpyridinium chloride precipitable acid glycosaminoglycans were determined. Further, the glyeosaminoglycan pattern of the epiphyseal plate and the incorporation of asS-sulphate into the glycosaminoglycans of bone tissue and epiphyseal cartilage after administration of asS-sulphate in vivo was studied.In compact bone tissue, the hexosamines corresponding to acid glycosaminoglycans constituted approximately one third of the total hexosamine concentration and approximately 0.0510.06% of the total dry weight. The main component of the acid glycosaminoglycans in bone was chondroitin-4-sulphate. This was sulphated to a higher degree and also of a higher molecular weight than the chondroitin sulphate of the epiphyseal cartilage, which in accordance with earlier investigations was found to have infrared characteristics of both chondroitin-4-sulphate and chondroitin-6-sulphate, with the former dominating. The molecular weights of the main part of bone chondroitin sulphate ranged from approximately 45,000 to 56,000. A small component of the bone glycosaminoglycans was hyaluronic acid.Large regularly recurring differences in the specific activity of fractions with differences in molecular weight in the chondroitin sulphate of bone tissue and epiphyseal cartilage were noted.Treatment of the dogs with parathyroid extract gave no effect on the molecular weights of the chondroitin sulphate of the bone matrix or of the epiphyseal cartilage. Nor was there any unequivocal effect on the concentrations of total hexosamines or on the acid glycosaminoglycans. No evident stimulatory or depressant effect on the incorporation of 3~S-sulphate into the chondroitin sulphate or in the molecular distribution of newly sulphated and/or synthesized molecules of the chondroitin sulphate within these tissues oceured.
